← Back to search
1l6t

STRUCTURE OF ALA24/ASP61 TO ASP24/ASN61 SUBSTITUTED SUBUNIT C OF ESCHERICHIA COLI ATP SYNTHASE

Method: SOLUTION NMR Dmax: 50.0 Å Quality: REASONABLE
▼

1. Protein Identity and Related Structures Protein Identity & Related Structures

ATP SYNTHASE C CHAIN

Escherichia coli

UniProt P68699

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count Chain A； UniProt 1–79 Mutation：A24D, D61N No other associated polymer SOLUTION NMR NMR measurement conditions：pH 5；300 K；Ionic strength (raw mmCIF value) 50 mM NACL；Pressure ATMOSPHERIC NMR sample composition：2.0 MM SUBUNIT C, 50 MM NACL, PH 5.0 | CDCl3:CD3OH:H20=4:4:1 Resolution not provided

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB Difference from Current Entry 1L6T Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1A91 SUBUNIT C OF THE F1FO ATP SYNTHASE OF ESCHERICHIA COLI; NMR, 10 STRUCTURES Deposited 1998-04-15 Different mutation/modification Different experimental conditions Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–79（79 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 5；300 K
Resolution not provided
1ATY DETERMINATION OF LOCAL PROTEIN STRUCTURE BY SPIN LABEL DIFFERENCE 2D NMR: THE REGION NEIGHBORING ASP61 OF SUBUNIT C OF THE F1FO ATP SYNTHASE Deposited 1994-10-05 Different mutation/modification Different experimental conditions Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–79（79 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR mmCIF provides none of the parsed conditions Resolution not provided
1C0V SUBUNIT C OF THE F1FO ATP SYNTHASE OF ESCHERICHIA COLI; NMR, 10 STRUCTURES Deposited 1999-07-22 Different mutation/modification Different experimental conditions Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–79（79 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 5；300 K；Pressure 1
NMR sample composition 4:4:1
Resolution not provided
1C17 A1C12 SUBCOMPLEX OF F1FO ATP SYNTHASE Deposited 1999-07-20 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Assembly 1 Protein heterocomplex Heteromer；Protein × 13 PDB declaration: tridecameric
Chain A 1–79（79 aa）
Chain B 1–79（79 aa）
Chain C 1–79（79 aa）
Chain D 1–79（79 aa）
Chain E 1–79（79 aa）
Chain F 1–79（79 aa）
Chain G 1–79（79 aa）
Chain H 1–79（79 aa）
Chain I 1–79（79 aa）
Chain J 1–79（79 aa）
Chain K 1–79（79 aa）
Chain L 1–79（79 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 5；300 K；Ionic strength (raw mmCIF value) 50 mM；Pressure AMBIENT
NMR measurement conditions pH 8；300 K；Ionic strength (raw mmCIF value) 50 mM；Pressure AMBIENT
NMR sample composition 1 MM SUBUNIT C
Resolution not provided
1C99 ASP61 DEPROTONATED FORM OF SUBUNIT C OF THE F1FO ATP SYNTHASE OF ESCHERICHIA COLI Deposited 1999-04-30 Different construct Different mutation/modification Different experimental conditions Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–79（79 aa） Fragment：subunit c
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 8；300 K
Resolution not provided
1IJP Solution Structure of Ala20Pro/Pro64Ala substituted subunit c of Escherichia coli ATP synthase Deposited 2001-04-27 Different construct Different mutation/modification Different experimental conditions Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–79（79 aa） Fragment：subunit c
Mutation：A20P, P64A No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 5；300 K；Ionic strength (raw mmCIF value) 50 mM NaCl；Pressure atmospheric
NMR sample composition 2.2 mM subunit c, 50 mM NaCl, pH 5.0 | CDCl3:CD3OD:D2O=4:4:1 or CDCl3:CD3OH:H2O=4:4:1
Resolution not provided
4UTQ A structural model of the active ribosome-bound membrane protein insertase YidC Deposited 2014-07-22 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain Z 1–79（79 aa） Fragment：MEMBRANE DOMAIN
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM vitrification conditions Cryogen ETHANE；VITRIFICATION 1 -- CRYOGEN- ETHANE, INSTRUMENT- FEI VITROBOT MARK IV,
Resolution 8.00 Å

7 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ATPL_ECOLI
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–79； UniProt 1–79

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

SAXS profile for 1l6t

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1l6t
Download Download
▼

2. Structure Basics 2. Structure Basics

Entry ID entry_id1l6t
Deposition date deposition_date2002-03-13
Structure title titleSTRUCTURE OF ALA24/ASP61 TO ASP24/ASN61 SUBSTITUTED SUBUNIT C OF ESCHERICHIA COLI ATP SYNTHASE
Keywords keywordsTRANSMEMBRANE HELIX, HYDROLASE; HYDROLASE
Experimental Method methodSOLUTION NMR
▼

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier18.33 Å
Radius of gyration Rg (electron density) rg_electron18.56 Å
Forward intensity I(0) i079141400.00
Molecular weight molecular_weight82801.0 kDa
Excluded volume excluded_volume107220 ų
Envelope volume envelope_volume19311 ų
Hydration-shell volume shell_volume9610 ų
Envelope diameter envelope_diameter70.2 Å
Shell Rg shell_rg23.21 Å
Envelope Rg envelope_rg20.63 Å
Shape Rg shape_rg18.53 Å
Total Rg total_rg18.88 Å
Total atoms total_atoms11970
Residues n_residues790
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3
▼

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax50.0 Å
Rg (real space) rg_real16.99 Å
Rg uncertainty (real space) rg_real_error0.14 Å
I(0) (real space) i0_real7.5600e+07
I(0) uncertainty (real space) i0_real_error7.8580e+05
Rg (reciprocal space) rg_reciprocal18.73 Å
I(0) (reciprocal space) i0_reciprocal79140000.0000
Solution quality estimate total_estimate0.5984
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary13.5 Å
Skewness Skewness skewness0.433
Kurtosis Kurtosis kurtosis-0.756
Angular range angular_range— – 0.4350 Å−1
Current regularization parameter α current_alpha3.1110
Highest regularization parameter α highest_alpha27130.0000
Real-space data points n_real_points75
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.001; Oscil: 0.845; Stabil: 0.962; Sysdev: 0.000; Positv: 1.000; Valcen: 0.371; Smooth: 0.000
▶

5. Crystallography and Experiment 5. Crystallography & Experiment

▶

6. Entities and Polymers Entities & Polymers (1)

▼

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1l6ta_
Class classf — Membrane and cell surface proteins and peptides
Fold Fold foldf.17 — Transmembrane helix hairpin
Superfamily Superfamily superfamilyf.17.1 — Rotary ATPase ring subunits
Family Family familyf.17.1.1 — F1F0 ATP synthase subunit C or V-type proton ATPase subunit c

CATH v4.4 (1 domains)

Domain ID domain_id1l6tA00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology20 — F1FO ATP Synthase
Homologous superfamily homologous superfamily10 — F1F0 ATP synthase subunit C
▶

8. Citations (1)

▶

9. Files and Curves (10)